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The tetrameric L27 domain complex as an organization platform for supramolecular assemblies
Wei Feng1, Jia-Fu Long, Jing-Song Fan
1Department of Biochemistry, Molecular Neuroscience Center, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, China.
Nature Structural & Molecular Biology
|March 30, 2004
Summary
The L27 domain, a key protein interaction module, forms tetrameric complexes. This structure explains how L27 domains polymerize scaffold proteins for cell polarity.
Area of Science:
- Structural Biology
- Molecular Cell Biology
Background:
- The L27 domain is a protein interaction module found in scaffold proteins.
- It plays a role in organizing protein assemblies for cell polarity.
Purpose of the Study:
- To determine the high-resolution NMR structure of a tetrameric L27 domain complex.
- To provide a mechanistic explanation for L27 domain-mediated polymerization.
Main Methods:
- High-resolution Nuclear Magnetic Resonance (NMR) spectroscopy.
- Structural analysis of a tetrameric complex of SAP97-mLin-2 L27 domains.
Main Results:
- The structure reveals a tetrameric complex formed by two L27 domain heterodimers.
- Each heterodimer consists of a four-helical bundle formed by the first two a-helices.
- A second four-helical bundle formed by the third a-helices of each L27 domain assembles the heterodimers into a tetramer.
Conclusions:
- The determined structure elucidates the mechanism of L27 domain polymerization.
- This polymerization is essential for assembling supramolecular complexes in asymmetric cells.